4qpe

X-ray diffraction
2Å resolution

Crystal structure of Aminopeptidase N in complex with N-cyclohexyl-1,2-diaminoethylphosphonic acid

Released:

Function and Biology Details

Reaction catalysed:
Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide.
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-191698 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aminopeptidase N Chain: A
Molecule details ›
Chain: A
Length: 870 amino acids
Theoretical weight: 98.96 KDa
Source organism: Neisseria meningitidis MC58
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9JYV4 (Residues: 1-867; Coverage: 100%)
Gene names: NMB1416, pepN
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: R3
Unit cell:
a: 224.495Å b: 224.495Å c: 57.951Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.173 0.171 0.202
Expression system: Escherichia coli BL21(DE3)